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- Currently displaying 26681 - 26700 of 29614 publications
Cumulative reaction probabilities for H+H2→H2+H from a knowledge of the anharmonic force field
Chemical Physics Letters
(1992)
192
407
(doi: 10.1016/0009-2614(92)85491-r)
The detection of weak heteronuclear coupling between spin 1 and spin nuclei in MAS NMR; 14N/13C/1H triple resonance experiments
Chemical Physics Letters
(1992)
192
379
(doi: 10.1016/0009-2614(92)85486-t)
A digital interface for phase control of PTS-300 synthesizers
Journal of Magnetic Resonance (1969)
(1992)
97
607
(doi: 10.1016/0022-2364(92)90039-a)
TOTAL SYNTHESIS OF THE CARBOXYLIC-ACID IONOPHORE ANTIBIOTIC CP-61,405 (ROUTIENNOCIN)
Synlett
(1992)
1992
395
(doi: 10.1055/s-1992-21357)
TOTAL SYNTHESIS OF THE CARBOXYLIC-ACID IONOPHORE ANTIBIOTIC CP-61,405 (ROUTIENNOCIN) - PREPARATION OF THE INHERENT SPIROKETAL UNIT VIA A REVERSE COUPLING PROCESS
Synlett
(1992)
1992
399
(doi: 10.1055/s-1992-21358)
INFRARED ULTRAVIOLET DOUBLE-RESONANCE MEASUREMENTS ON THE RELAXATION OF ROTATIONAL ENERGY IN THE (3(1), 2(1)4(1)5(1)) FERMI RESONANCE STATES OF C2H2
Chemical Physics Letters
(1992)
191
574
(doi: 10.1016/0009-2614(92)85591-W)
OBSERVATION OF SURFACE ACOUSTIC PHONON RESONANCES - APPLICATIONS TO THE CO+O2 OSCILLATORY REACTION ON PT(100)
Chemical Physics Letters
(1992)
191
379
(doi: 10.1016/0009-2614(92)85395-q)
Preliminary communication: Unexpected length dependence of die solubility of chain molecules
Molecular Physics
(1992)
75
983
(doi: 10.1080/00268979200100761)
Cyclocholates: Synthesis and Ion Binding
Tetrahedron Letters
(1992)
33
2071
(doi: 10.1016/0040-4039(92)88145-u)
An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate.
J Mol Biol
(1992)
224
749
(doi: 10.1016/0022-2836(92)90559-3)
Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability.
Journal of molecular biology
(1992)
224
759
(doi: 10.1016/0022-2836(92)90560-7)
The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding.
J Mol Biol
(1992)
224
771
(doi: 10.1016/0022-2836(92)90561-w)
The folding of an enzyme
Journal of Molecular Biology
(1992)
224
783
(doi: 10.1016/0022-2836(92)90562-x)
The folding of an enzyme V. solH2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: Complementarity to and agreement with protein engineering studies
J Mol Biol
(1992)
224
837
(doi: 10.1016/0022-2836(92)90565-2)
The folding of an enzyme
Journal of molecular biology
(1992)
224
847
(doi: 10.1016/0022-2836(92)90566-3)
Dissection of an enzyme by protein engineering. The N and C-terminal fragments of barnase form a native-like complex with restored enzymic activity.
J Mol Biol
(1992)
224
741
(doi: 10.1016/0022-2836(92)90558-2)
The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure.
J Mol Biol
(1992)
224
805
(doi: 10.1016/0022-2836(92)90563-y)
THE FOLDING OF AN ENZYME .4. STRUCTURE OF AN INTERMEDIATE IN THE REFOLDING OF BARNASE ANALYZED BY A PROTEIN ENGINEERING PROCEDURE
Journal of molecular biology
(1992)
224
819
(doi: 10.1016/0022-2836(92)90564-Z)
Co-operative interactions during protein folding.
J Mol Biol
(1992)
224
733
(doi: 10.1016/0022-2836(92)90557-Z)
